ID A0A0R2QDZ8_9ACTN Unreviewed; 343 AA.
AC A0A0R2QDZ8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=3-isopropylmalate dehydrogenase {ECO:0000313|EMBL:KRO45754.1};
DE EC=1.1.1.85 {ECO:0000313|EMBL:KRO45754.1};
GN ORFNames=ABR56_01455 {ECO:0000313|EMBL:KRO45754.1};
OS Acidimicrobium sp. BACL27 MAG-120823-bin4.
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Acidimicrobiaceae; Acidimicrobium.
OX NCBI_TaxID=1655564 {ECO:0000313|EMBL:KRO45754.1, ECO:0000313|Proteomes:UP000050870};
RN [1] {ECO:0000313|EMBL:KRO45754.1, ECO:0000313|Proteomes:UP000050870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL17 MAG-120823-bin4 {ECO:0000313|EMBL:KRO45754.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate
CC + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.1.1.85;
CC Evidence={ECO:0000256|ARBA:ARBA00000624};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRO45754.1}.
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DR EMBL; LIAO01000312; KRO45754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2QDZ8; -.
DR Proteomes; UP000050870; Unassembled WGS sequence.
DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR PANTHER; PTHR43275; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 1.
DR PANTHER; PTHR43275:SF1; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Oxidoreductase {ECO:0000313|EMBL:KRO45754.1}.
FT DOMAIN 15..335
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 343 AA; 36262 MW; E1B59E25C68A9D93 CRC64;
MSKHVVTNNS VAGHRVAVIG GDGIGPEVLA EALKVVGATG VKLATTSFDL GGARYLRDGE
VLSDATLGEL RKFDAILLGA VGTPGVPPGV IERGLLLKMR FELDLYINRR PFSGTAPGHT
KPHDFVVIRE NTEGPYVGEG GVLRRGTPDE VATQGSVNTA KGVERCVRYA FELARTRSRK
HLTLVHKTNV LTFAGDLWQR TFDRVAKEFT DVATAYNHVD AACIYFVQDP HRFDVIVTDN
LFGDILTDLG GAVSGGIGVA SSANLNPTRS GPSMFEPVHG SAPDIAGKGV ANPVAAILSA
AHMLEFLGET KAAEILRDAC AEPVSGSTVA VGDEIARRVK ANI
//
